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抗Mouse (Murine) PDIA2 抗体:
抗Human PDIA2 抗体:
抗Rat (Rattus) PDIA2 抗体:
Human Polyclonal PDIA2 Primary Antibody for ELISA, WB - ABIN547889
Uehara, Nakamura, Yao, Shi, Gu, Ma, Masliah, Nomura, Lipton: S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. in Nature 2006
Polyclonal PDIA2 Primary Antibody for IHC (fro), IF - ABIN540891
Safran, Leonard: Characterization of a N-bromoacetyl-L-thyroxine affinity-labeled 55-kilodalton protein as protein disulfide isomerase in cultured glial cells. in Endocrinology 1991
Show all 3 Pubmed References
Rotavirus-protein disulfide isomerase interaction was demonstrated in vitro as well as inMA104 cells and intestinal villi from suckling mice.
Data show that diabetic mice had a worse postinfarction remodeling associated with an altered protein disulfide isomerase (PDI). redox state.
The absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer.
Elevated Pdi expression is cis regulated and is not linked to diabetes susceptibility.
Galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface.
PDI overexpression is associated with Multiple Myeloma.
Tissue factor-regulated vascular smooth cell migration and microvessel formation is under the control of the ER-protein PDIA2.
It was found that PDI interacts with dengue virus nonstructural protein 1 (NS1) intracellularly as well as on the surface in the lipid raft domain.
Data show that cell surface disulfide isomerase (PDI) expression and function regulate the capacity of natriuretic peptides to generate cyclic guanosine monophosphate (cGMP) through interaction with their receptors.
The redox-regulated open/closed conformational switch of hPDI endows the protein with versatile target-binding capacities for its enzymatic and chaperone functions.
These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation.
PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism.
Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC).
GPx7 is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys mechanism in which GSH and PDI are alternative substrates.
Human major histocompatibility complex class 1 antigens (HLA-A,B,C) are potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation.
Data indicate that apoptosis induced by misfolded PrP proteins could be regulated by protein disulfide isomerase (PDI) via mitochondrial dysfunction.
The hydrogen bond, formed between the 3-hydroxyl group of Estradiol (E(2)) (donor) and pancreas-specific protein disulfide isomerase's His278 (acceptor), is indispensable for its binding.
PDI is required to support Nox1/redox and GTPase-dependent VSMC migration.
PDI exhibits unfoldase activity for proinsulin, increasing retention of proinsulin within the ER of pancreatic beta-cells
Data show that diabetic patients had a greater number of transferase-mediated dUTP nick-end labeling-positive cells than nondiabetic patients despite a greater myocardial protein disulfide isomerase (PDI)expression suggesting altered PDI function.
surface-associated PDI is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation
mechanistic insights into the redox-regulated chaperone activity of human PDI.
the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha.
tein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation.
Protein disulfide isomerases (EC 18.104.22.168), such as PDIP, are endoplasmic reticulum (ER) resident proteins that catalyze protein folding and thiol-disulfide interchange reactions (Desilva et al., 1996
protein disulfide isomerase family A, member 2
, protein disulfide isomerase A2
, Protein disulfide-isomerase A2
, protein disulfide-isomerase A2-like
, protein disulfide isomerase (pancreas) like
, protein disulfide isomerase, pancreatic
, protein disulfide-isomerase A2
, Rho GDP dissociation inhibitor gamma
, pancreas-specific protein disulfide isomerase
, pancreatic protein disulfide isomerase
, protein disulfide isomerase-associated 2
, protein disulfide isomerase associated 2